Particle-Based Microrheology As a Tool for Characterizing Protein-Based Materials

Meleties, Michael; Martineau, Rhett L.; Gupta, Maneesh K.; Montclare, Jin Kim

doi:10.1021/acsbiomaterials.2c00035

Cited by 10 publications

(6 citation statements)

References 71 publications

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“…Previously, condensate viscosities between ∼ 0.1 Pa.s and 200 Pa.s have been reported, this range is well accommodated by this technique, plus has the potential to measure much stiffer systems, with moduli up to 10 4 . 45 However, one downside compared to video particle tracking is the loss of spatial information. This means interesting heterogeneity across a sample could be obscured.…”

Section: Resultsmentioning

confidence: 99%

Viscoelasticity of globular protein-based biomolecular condensates

Fisher,

Obermeyer

2023

Preprint

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The phase separation of biomolecules into biomolecular condensates has emerged as a ubiquitous cellular process. Understanding how intrinsically disordered protein sequence controls condensate formation and material properties has led to the development of functional synthetic condensates. However, it is also crucial to understand the impact of folded domains on condensate properties. We set out to determine how distribution of sticker interactions across a globular protein contributes to network properties of hybrid protein-polymer condensates and to what extent globular protein-polyelectrolyte coacervates differ from those formed from two linear components. We designed three variants of green fluorescent protein with different charge patterning and used dynamic light scattering microrheology to measure the viscoelastic spectrum over a timescale of 10-6to 10 seconds, elucidating the response of protein condensates in this range for the first time. We further showed that the phase behavior and rheological characteristics of the condensates varied as a function of both protein charge distribution and polymer/protein ratio. Together, this work provides an increase in fundamental understanding of complex dynamic materials across length-scales.

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Section: Resultsmentioning

confidence: 99%

Viscoelasticity of globular protein-based biomolecular condensates

Fisher,

Obermeyer

2023

Preprint

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“…Microrheology can usually be used to trace the motion of colloidal particles at the scale of 0.1–10 μm. By detecting the Brownian motion of droplets, the displacement of particles can be accurately detected and the microrheological behavior of liquids can be analyzed [ 48 ]. The microrheology could reflect the structure and viscoelastic changes of the emulsion system by the mean square displacement (MSD) of the emulsion droplet as the formula of the de-correlation time.…”

Section: Resultsmentioning

confidence: 99%

The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties

Wu,

He,

Feng

et al. 2023

Foods

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It has been proven that high-pressure homogenization (HPH) could improve the functional properties of proteins by modifying their structure. This study researched the effect of HPH on the structural and functional properties of whey-soy dual-protein (Soy Protein Isolation-Whey Protein Isolation, SPI-WPI). Different protein solution samples were treated with HPH at 30, 60, 90, 120 and 150 MPa, and the structure changed under different pressures was analyzed by measuring particle size, zeta potential, Fourier infrared spectrum (FTIR), fluorescence spectrum and scanning electron microscope (SEM). The results showed that HPH significantly reduced the particle size of SPI-WPI, changed the secondary and tertiary structures and improved the hydrophobic interaction between molecules. In addition, HPH significantly improved the solubility and emulsification of all proteins, and the improvement effect on SPI-WPI was significantly better than SPI and WPI. It was found that SPI-WPI treated with 60 MPa had the best physicochemical properties. Secondly, we researched the effect of HPH by 60 MPa on the emulsion properties of SPI-WPI. In this study, the SPI-WPI had the lowest surface tension compared to a single protein after HPH treatment. The emulsion droplet size was obviously decreased, and the elastic properties and physical stability of SPI-WPI emulsion were significantly enhanced. In conclusion, this study will provide a theoretical basis for the application of HPH in modifying the structure of dual-protein to improve its development and utilization in liquid specialty food.

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“…The fact that the gel we produced can be easily seeded with nanoparticles, is promising for possible application in drug delivery and tissue regeneration [ 8 , 64 , 65 ]. Particularly appealing, will be to study the dynamics of small objects, such as particles of different sizes [ 39 , 66 ], bacteria, viruses, and cells, embedded in weak gels, where microscopic motion is never completely arrested.…”

Section: Discussionmentioning

confidence: 99%

“…While the micro-structure of peptide-based hydrogels, and their mechanical properties, have been extensively studied, with several techniques [ 21 , 35 , 36 ], such as rheometry [ 37 , 38 , 39 ], static small-angle scattering [ 40 , 41 ], and transmission electron microscopy [ 42 , 43 ], the kinetics of aggregation and the following gelation have been investigated much less. A relatively small number of works have investigated the assembly process using circular dichroism (CD) [ 44 , 45 , 46 , 47 ], Fourier-transform infrared spectroscopy (FTIR) [ 48 ], and thioflavin T fluorescence [ 34 , 49 ].…”

Section: Introductionmentioning

confidence: 99%

A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides

Buzzaccaro

Ruzzi

Gelain

et al. 2023

Gels

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Self-assembling peptides (SAPs) have been increasingly studied as hydrogel–former gelators because they can create biocompatible environments. A common strategy to trigger gelation, is to use a pH variation, but most methods result in a change in pH that is too rapid, leading to gels with hardly reproducible properties. Here, we use the urea–urease reaction to tune gel properties, by a slow and uniform pH increase. We were able to produce very homogeneous and transparent gels at several SAP concentrations, ranging from c=1g/L to c=10g/L. In addition, by exploiting such a pH control strategy, and combining photon correlation imaging with dynamic light scattering measurements, we managed to unravel the mechanism by which gelation occurs in solutions of (LDLK)3-based SAPs. We found that, in diluted and concentrated solutions, gelation follows different pathways. This leads to gels with different microscopic dynamics and capability of trapping nanoparticles. At high concentrations, a strong gel is formed, made of relatively thick and rigid branches that firmly entrap nanoparticles. By contrast, the gel formed in dilute conditions is weaker, characterized by entanglements and crosslinks of very thin and flexible filaments. The gel is still able to entrap nanoparticles, but their motion is not completely arrested. These different gel morphologies can potentially be exploited for controlled multiple drug release.

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Particle-Based Microrheology As a Tool for Characterizing Protein-Based Materials

Cited by 10 publications

References 71 publications

Viscoelasticity of globular protein-based biomolecular condensates

Viscoelasticity of globular protein-based biomolecular condensates

The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties

A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides

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